Phospho-PAK2 (Ser20) refers to the p21-activated kinase 2 (PAK2) protein that has been phosphorylated at the serine residue number 20. PAK2 is a serine/threonine kinase involved in various signaling pathways, including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis, and proliferation. It acts as a downstream effector of the small GTPases CDC42 and RAC1. When active, CDC42 and RAC1 bind to PAK2, causing a conformational change and subsequent autophosphorylation on several serine and/or threonine residues, including Ser20. Phosphorylation at Ser20 is significant because it can affect the activation state of PAK2 and its ability to interact with other proteins. For instance, phosphorylation of PAK2 at Ser20 has been implicated in the regulation of the actin cytoskeleton and T cell receptor (TCR) signaling, which are crucial for normal thymocyte development and maturation. Additionally, the phosphorylation status of PAK2 can serve as a marker for cellular processes and can be detected using specific antibodies designed to recognize the phosphorylated form of the protein.
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